Structure of PDB 3t2d Chain A

Receptor sequence
>3t2dA (length=390) Species: 444157 (Pyrobaculum neutrophilum V24Sta) [Search protein sequence]
MRVTVSIIKADVGGFPGHAHVHPKMLEYAAAKLKEAQKRGVIIDYFVYNV
GDDISLLMTHTKGEDNKDIHGLAWETFKEVTDQIAKRFKLYGAGQDLLKD
AFSGNIRGMGPQVAEMEFEERPSEPIIAFAADKTEPGAFNLPLYKMFADP
FTTAGLVIDPSMHEGFIFEVLDVVEHKVYLLKTPEDAYSLLGLIGTTGRY
IIRKVFRRADGAPAAANSVERLSLIAGRYVGKDDPVLLVRAQSGLPAVGE
VLEAFAHPHLVHGWMRGSHAGPLMPARFISVDPERRIAIGPKMTRFDGPP
KVGALGFQLHEGYLEGGVDLFDDPAFDYVRQTAAQIADYIRRMGPFQPHR
LPPEEMEYTALPKILAKVKPYPADQYEKDRKKYIEAVVKG
3D structure
PDB3t2d Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase.
ChainA
Resolution1.36 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
4.1.2.13: fructose-bisphosphate aldolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A D52 D53 D132 D234 D52 D53 D132 D234
BS02 MG A D11 H18 D52 Q95 D11 H18 D52 Q95
BS03 MG A D233 D234 D233 D234
BS04 P6F A H18 D52 Y91 Q95 S103 G104 N105 K133 D233 D234 M265 R266 D297 Y358 H18 D52 Y91 Q95 S103 G104 N105 K133 D233 D234 M265 R266 D297 Y358
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004332 fructose-bisphosphate aldolase activity
GO:0016787 hydrolase activity
GO:0016829 lyase activity
GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0006094 gluconeogenesis

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Molecular Function
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Biological Process
External links
PDB RCSB:3t2d, PDBe:3t2d, PDBj:3t2d
PDBsum3t2d
PubMed21983965
UniProtB1YAL1|FBPAP_PYRNV Fructose-1,6-bisphosphate aldolase/phosphatase (Gene Name=fbp)

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